title: Applications of snake venom components to modulate integrin activities in cell-matrix interactions.
abstract: Snake venom proteins are broadly investigated in the different areas of life science. Direct interaction of these compounds with cells may involve a variety of mechanisms that result in diverse cellular responses leading to the activation or blocking of physiological functions of the cell. In this review, the snake venom components interacting with integrins will be characterized in context of their effect on cellular response. Currently, two major families of snake venom proteins are considered as integrin-binding molecules. The most attention has been devoted to the disintegrin family, which binds certain types of integrins through specific motifs recognized as a tri-peptide structurally localized on an integrin-binding loop. Other snake venom integrin-binding proteins belong to the C-type lectin family. Snake venom molecules bind to the cellular integrins resulting in a modulation of cell signaling and in consequence, the regulation of cell proliferation, migration and apoptosis. Therefore, snake venom research on the integrin-binding molecules may have significance in biomedicine and basic cell biology.
authors.affiliation: Temple University, Department of Biology, Philadelphia, PA 19122, USA. cmarcink@temple.edu
authors.forename: Cezary
authors.initials: C
authors.lastname: Marcinkiewicz
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019483:Disintegrins / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D005109:Extracellular Matrix / Q000737:chemistry / Q000187:drug effects* / Q000378:metabolism*; D006801:Humans; D016023:Integrins / Q000378:metabolism*; D008969:Molecular Sequence Data; D015398:Signal Transduction; D012910:Snake Venoms / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*
chemical_list: D019483:Disintegrins; D016023:Integrins; D012910:Snake Venoms
keywords: Angiogenesis; C-lectin type proteins; Cell adhesion; Disintegrins; Integrins